人胰岛素两种二硫键异构体的合成及生物活性：[A7-A11,A6-B7-胱氨酸]-和[A6-A7,A11-B7-胱氨酸]胰岛素（人） - Suppr

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超能文献

Synthesis and biological activity of two disulphide bond isomers of human insulin: [A7-A11,A6-B7-cystine]- and [A6-A7,A11-B7-cystine]insulin (human).

作者信息

Sieber P, Eisler K, Kamber B, Riniker B, Rittel W, Märki F, de Gasparo M

出版信息

Hoppe Seylers Z Physiol Chem. 1978 Jan;359(1):113-23. doi: 10.1515/bchm.1978.359.1.113.

DOI:10.1515/bchm.1978.359.1.113

PMID:627397

Abstract

摘要

相似文献

Synthesis and biological activity of two disulphide bond isomers of human insulin: [A7-A11,A6-B7-cystine]- and [A6-A7,A11-B7-cystine]insulin (human).人胰岛素两种二硫键异构体的合成及生物活性：[A7-A11,A6-B7-胱氨酸]-和[A6-A7,A11-B7-胱氨酸]胰岛素（人）

Hoppe Seylers Z Physiol Chem. 1978 Jan;359(1):113-23. doi: 10.1515/bchm.1978.359.1.113.

A protein caught in a kinetic trap: structures and stabilities of insulin disulfide isomers.处于动力学陷阱中的一种蛋白质：胰岛素二硫键异构体的结构与稳定性

Biochemistry. 2002 Dec 17;41(50):14700-15. doi: 10.1021/bi0202981.

Determination of disulfide bond arrangement in bombyxin-IV, an insulin superfamily peptide from the silkworm, Bombyx mori, by combination of thermolysin digestion of natural peptide and selective synthesis of disulfide bond isomers.通过天然肽的嗜热菌蛋白酶消化与二硫键异构体的选择性合成相结合的方法，确定家蚕胰岛素超家族肽家蚕素-IV中的二硫键排列。

J Protein Chem. 1992 Feb;11(1):13-20. doi: 10.1007/BF01025087.

Flexibility exists in the region of [A6-A11, A7-B7] disulfide bonds during insulin precursor folding.胰岛素前体折叠过程中，[A6 - A11，A7 - B7]二硫键区域存在灵活性。

J Biochem. 2004 Jan;135(1):1-6. doi: 10.1093/jb/mvg134.

Replacement of the interchain disulfide bridge-forming amino acids A7 and B7 by glutamate impairs the structure and activity of insulin.将形成链间二硫键的氨基酸A7和B7替换为谷氨酸会损害胰岛素的结构和活性。

Biol Chem. 2004 Dec;385(12):1171-5. doi: 10.1515/BC.2004.151.

Role of disulfide bonds in the structure and activity of human insulin.二硫键在人胰岛素结构和活性中的作用。

Mol Cells. 2003 Dec 31;16(3):323-30.

Semisynthesis of A6-A11 lactam insulin.A6-A11 内酰胺胰岛素的半合成。

J Pept Sci. 2024 Feb;30(2):e3542. doi: 10.1002/psc.3542. Epub 2023 Sep 11.

Dissecting the role of disulfide bonds on the amyloid formation of insulin.解析二硫键在胰岛素淀粉样纤维形成中的作用。

Biochem Biophys Res Commun. 2012 Jun 29;423(2):373-8. doi: 10.1016/j.bbrc.2012.05.133. Epub 2012 Jun 1.

Insulin in motion: The A6-A11 disulfide bond allosterically modulates structural transitions required for insulin activity.胰岛素的运动：A6-A11 二硫键变构调节胰岛素活性所需的结构转变。

Sci Rep. 2017 Dec 8;7(1):17239. doi: 10.1038/s41598-017-16876-3.

Selective cleavage of one disulfide bond in insulin: preparation and properties of insulin A7-B7-di-S-sulfonate.胰岛素中一个二硫键的选择性裂解：胰岛素A7-B7-二硫代磺酸盐的制备与性质

Hoppe Seylers Z Physiol Chem. 1973 Feb;354(2):147-55. doi: 10.1515/bchm2.1973.354.1.147.

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Structural Lessons From the Mutant Proinsulin Syndrome.从突变胰岛素综合征中得到的结构教训。

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Probing the correlation between insulin activity and structural stability through introduction of the rigid A6-A11 bond.通过引入刚性 A6-A11 键探究胰岛素活性与结构稳定性之间的相关性。

J Biol Chem. 2018 Jul 27;293(30):11928-11943. doi: 10.1074/jbc.RA118.002486. Epub 2018 Jun 13.

Insulin-like peptide 3 expressed in the silkworm possesses intrinsic disulfide bonds and full biological activity.蚕中表达的胰岛素样肽 3 具有内在的二硫键和完整的生物活性。

Sci Rep. 2017 Dec 11;7(1):17339. doi: 10.1038/s41598-017-17707-1.

Diabetes mellitus due to the toxic misfolding of proinsulin variants.因胰岛素原变体的毒性错误折叠导致的糖尿病。

FEBS Lett. 2013 Jun 27;587(13):1942-50. doi: 10.1016/j.febslet.2013.04.044. Epub 2013 May 10.

Insulin: a small protein with a long journey.胰岛素：一种具有漫长旅程的小蛋白质。

Protein Cell. 2010 Jun;1(6):537-51. doi: 10.1007/s13238-010-0069-z.

Proinsulin misfolding and diabetes: mutant INS gene-induced diabetes of youth.胰岛素前体错误折叠与糖尿病：突变 INS 基因导致的青少年糖尿病。

Trends Endocrinol Metab. 2010 Nov;21(11):652-9. doi: 10.1016/j.tem.2010.07.001. Epub 2010 Aug 18.

Deciphering the hidden informational content of protein sequences: foldability of proinsulin hinges on a flexible arm that is dispensable in the mature hormone.破译蛋白质序列中的隐藏信息内容：胰岛素原的折叠性取决于一条灵活的臂，该臂在成熟激素中是可有可无的。

J Biol Chem. 2010 Oct 1;285(40):30989-1001. doi: 10.1074/jbc.M110.152645. Epub 2010 Jul 27.

Contribution of residue B5 to the folding and function of insulin and IGF-I: constraints and fine-tuning in the evolution of a protein family.残基 B5 对胰岛素和 IGF-I 折叠和功能的贡献：蛋白质家族进化中的约束和微调。

J Biol Chem. 2010 Feb 12;285(7):5040-55. doi: 10.1074/jbc.M109.062992. Epub 2009 Dec 3.

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